Asp-960/Glu-961 controls the movement of the C-terminal tail of the epidermal growth factor receptor to regulate asymmetric dimer formation.

ABSTRACT: The epidermal growth factor (EGF) receptor is a tyrosine kinase that dimerizes in response to ligand binding. Ligand-induced dimerization of the extracellular domain of the receptor promotes formation of an asymmetric dimer of the intracellular kinase domains, leading to stimulation of the tyrosine kinase activity of the receptor. We recently monitored ligand-promoted conformational changes within the EGF receptor in real time using luciferase fragment complementation imaging and showed that there was significant movement of the C-terminal tail of the EGF receptor following EGF binding (Yang, K. S., Ilagan, M. X. G., Piwnica-Worms, D., and Pike, L. J. (2009) J. Biol. Chem. 284, 7474-7482). To investigate the structural basis for this conformational change, we analyzed the effect of several

SUBMITTER: Yang KS 

PROVIDER: S-EPMC2911325 | biostudies-literature | 2010 Jul

REPOSITORIES: biostudies-literature